Inv(1) allotype: effect of immunoglobulin G heavy chain subtype on its expression

More protein is required to detect the Inv(1) antigen carried in the light chain of immunoglobulin G molecules when the light chain is combined with a gamma2 heavy chain than when it is combined with a gamma1 or gamma3 heavy chain. One of the four gamma2 heavy chains used in the experiment, however, was as efficient as the gamma1 and gamma3 chains, indicating that there may be two subtypes of gamma2. Inv(1) was more easily detected in one of the two light chains used in the experiment. This difference may be associated with the subtypes of the kappa chain derived from studies of the variable portion of the chain.     

Gammaglobulin factors (Gm and Inv) in New Guinea: anthropological significance

Analysis of the hereditary Gm and Inv gamma-globulin factors of 1669 New Guineans from the Morobe and Eastern Highlands districts and Bougainville Island demonstrates thatthe frequencies of the three Gm alleles present (Gm(a), GM(ab), and Gm(ax)) are similar in general to those in Mongoloids and in particular to those in Southeast Asians and Micronesians. The New Guinea frequencies are distinct from those in other populations, including Australian aborigines. Highly significant differences in frequencies of Gm and Inv alleles occur between Melanesian-and non-Austronesian-speaking New Guineans.     

2 types of lambda polypeptide chains in human immunoglobulins

Two antigenic subtypes of human lambda polypeptide chains were distinguished by rabbit antiserum produced to a lambda Bence Jones protein. Lambda Bence Jones proteins and G myeloma proteins with lambda light chains were identified as being in one or the other subtype. The Oz (+) lambda chain subtype is present in light chains from pooled normal human immunoglobulin G and in whole normal immunoglobulin G molecules.     

Interactions of immunoglobulins G and M in the detection of the mammalian C-type virus cross-reactive antigen

The mammalian C-type tumor viruses share an antigenic determinant, gs-3, located on the major internal polypeptide of the virion. Detection of this determined in gel diffusion assays by antiserums prepared in rats by immunization with rat tumor homogenates carrying murine virus and serums prepared in a rabbit by immunization with purified murine gs antigen depended on antibodies present in the fractions containing immunoglobulins M and G. The immunoglobulin G fraction by itself precipitated only the homologous murine antigen. Neither fraction alone precipitated heterologous (cat, rat, or hamster) antigen (definition of the gs-3 reaction), while a mixture of the two fractions did. The gs-3 reaction was eliminated by treatment of the serums with beta-mercaptoethanol, also indicating a requirement for immunoglobulin M antibodies.     

Genetically determined antigen of the Ne subgroup of gamma-globulin: detection by precipitin analysis

A genetic antigen, Gm(n), has been described for the Ne subgroup of gamma-globulin previously devoid of Gm factors. It was detected by precipitin tests with a primate antiserum to Ne-type heavy chains. A relation to the Gm(b) antigens of the Vi subgroup and the Gm(f) and Gm(y) antigens of the We subgroup was apparent. The availablity of genetic antigens for the heavy chains of three subgroups of gamma-globulin with varying relationships in different populations offers an approach to the mapping of the genes concerned.     

Antigenic streptococcal components in acute glomerulonephritis

Fluorescein-labeled immunoglobulin G fractions from serums of patients with acute glomerulonephritis and from many normal serums stained the glomerular basement membrane and mesangium of renal tissue from patients with early acute glomerulonephritis; these serums did not stain the corresponding tissues from patients with any other kidney disease. Previous absorption of the serum fraction with frozen and thawed nephritogenic beta hemolytic streptococci abolished all staining. Other bacteria studied did not abolish the staining. Only the plasma membrane of the streptococcus absorbed the immunoglobulin G fraction; such absorption eliminated staining. Fluorescein-labeled antiserums against streptococcal plasma membrane had staining properties similar to patients' serums.     

Concanavalin A reaction with human normal immunoglobulin G and myeloma immunoglobulin G

Concanavalin A precipitated less than 5 percent of immunoglobulin G from human serum. It reacted with all of 42 myeloma serums of the immunoglobulin G type tested, but no more than approximately 50 percent of the total myeloma protein was ever precipitated. The fact that not all of the protein was precipitated and that the amounts precipitated varied from serum to serum may be interpreted as demonstrating heterogeneity of the carbohydrate in these myeloma proteins. Other glycoproteins precipitated by concanavalin A were identified, and subsequently separated from concanavalin A by chromatography.     

Plasma 3S gamma-1-globulin: identity with erythrocyte carbonic anhydrase B

The 3S (gamma1), 2S (gamma2), and 0.5S (gamma2) fractions of human plasma are heterogeneous in protein composition. Although each fraction contained a relatively small amount of protein antigenically related to the immunoglobulin light chains, most of the proteins were unrelated to immunogloublin G or its light chains. Of the 3S (gamma1)-globulins the greater part was immunochemically identical to carbonic anhydrase B and had carbonic anhydrase activity. These findings explain earlier reports of an immunochemical similarity between 3S (gamma1)-globulins and immunoglobulin light chains in spite of marked differences in amino acid and peptide composition between the two. Apparently not all plasma gamma-globulins are necessarily immunoglobulins.     

Immunoglobulin M and secretory immunoglobulin A: presence of a common polypeptide chain different from light chains

Unique polypeptide chains have been isolated from S-sulfonated light-chain fractions of human serum immunoglobulin M and colostral immunoglobulin A. Their electrophoretic mobilities, molecular weights, peptide maps, amino acid compositions, and antigenic determinants are very similar or perhaps identical but differ from those of light chains and secretory piece.     

Limited heterogeneity of gamma globulin in hypogammaglobulinemia

When serums of 11 patients with hypogammaglobulinemia were examined by acrylamide-gel electrophoresis, combined with diffusion analysis, for the gamma chain of immunoglobulin G, the electrophoretic distribution of immunoglobulin G differed from that of normal individuals. The differences consisted of limited heterogeneity and bimodal distributions of the proteins at times. Isolated immunoglobulin G from four of the patients showed similar phenomena. The findings indicate a deficient gene population in these patients.     

Complement-immunoglobulin relation: deficiency of C'1q associated with impaired immunoglobulin G synthesis

Concentration of the complement protein C'lq was determined immunochemically in serums of individuals with a wide variety of immunoglobulin abnormalities. A significant correlation was observed between decreased concentration of C'lq and deficient synthesis of immunoglobulin G; C'lq was particularly diminished in subjects with congenital, sex-linked (Bruton) agammaglobulinemia. In contrast, two to five times the normal concentration of C'lq was found in the serum of three patients with heavy chain disease (subtype immunoglobulin G3). No significant relation was found between C'lq and concentrations of immunoglobulins A and M.     

3种球囊霉属真菌对盆栽木薯生长影响

应用盆栽试验法,单独接种球囊霉属Glomus菌种：根内球囊霉G．intraradices（Gi）、木薯球囊霉Gmanihotis（Gm）和幼套球囊霉Getunicatum（Ge）菌剂及混合菌剂（2G）,检测不同接种条件下对盆栽木薯Manihot esculenta根系的侵染能力及其对木薯生长的影响．3个试验菌种均可与木薯形成疆南星型（Arum—type）丛枝菌根（arbuscular mycorrhiza,AM）,其中Gi和Gm均可在菌根内形成根内孢子．2G和Gi均显示较强的侵染能力,Gm在早期的侵染较慢,但在后期的感染率较高,Ge侵染能力最差．2G、Gi和Gm处理组木薯的高度生长均比非接种处理的对照组好,但只有2G处理组无论株高生长还是生物积累均达到显著水平,其他处理组差异不显著,Ge处理组木薯在叶部和根部生物量的积累有负向影响．     

Immunoglobulin M allotypes of the rabbit: identification of a second specificity

Rabbit antiserums, originally prepared to react specifically with rabbit immunoglobulin allotypes Ab5 and Ab6, also react with some normal rabbit serums that clearly do not contain Ab5 or Ab6 allotypes. This reaction is due to antigenic specificity present on rabbit immunoglobulin M(IgM) and not on rabbit immunoglobulin G.Serums that contain this IgM allotype do not react with an antiserum that reacts with the known rabbit IgM allotype, Ms1. This specificity may therefore be identified as a second rabbit IgM allotype, Ms2.     

NEW SERUM GROUP, GM(P)

The agglutination that occurs when rheumatoid arthritis serum Pond is added to erythrocytes sensitized with anti-D serum Moore is inhibited in the presence of some normal serums. The inhibitor, tentatively named Gm(p), is associated only with 7S gamma globulins and is apparently different from other previously defined serum groups. It is much more common in Caucasians than in Negroes, and probably is determined by a simple dominant gene.     

A novel, highly stable fold of the immunoglobulin binding domain of streptococcal protein G

The high-resolution three-dimensional structure of a single immunoglobulin binding domain (B1, which comprises 56 residues including the NH2-terminal Met) of protein G from group G Streptococcus has been determined in solution by nuclear magnetic resonance spectroscopy on the basis of 1058 experimental restraints. The average atomic root-mean-square distribution about the mean coordinate positions is 0.27 angstrom (A) for the backbone atoms, 0.65 A for all atoms, and 0.39 A for atoms excluding disordered surface side chains. The structure has no disulfide bridges and is composed of a four-stranded beta sheet, on top of which lies a long helix. The central two strands (beta 1 and beta 4), comprising the NH2- and COOH-termini, are parallel, and the outer two strands (beta 2 and beta 3) are connected by the helix in a +3x crossover. This novel topology (-1, +3x, -1), coupled with an extensive hydrogen-bonding network and a tightly packed and buried hydrophobic core, is probably responsible for the extreme thermal stability of this small domain (reversible melting at 87 degrees C).     

Shared antigens between Mycobacterium bovis (BCG) and other bacterial species

Antigens from Mycobacterium bovis and Listeria monocytogenes bind to serums from normal rabbits as well as from those immunized with unrelated bacteria, especially intracellular parasites. Binding is to the Fab portion of immunoglobulin G and is immunologically specific.     

Lupus nephritis: varying complement-fixing properties of immunoglobulin G antibodies to antigens of cell nuclei

Relative complement-fixing activity of antibodies to nuclear antigens, including DNA, were determined in serums of 15 patients with, and 65 patients without, active lupus nephritis, by comparing titers obtained in two methods. High complement-fixing activity of antibody was found in the nephritis group and low activity in the others. Results with immunoglobulin G fractions were similar.     

Subclasses of human immunoglobulin a based on differences in the alpha polypeptide chains

Antiserum from goats immunized with heavy polypeptide chains from a gammaA-type myeloma globulin was absorbed with serum from patients with selective absence of immunoglobulin A (gammaA). The resulting reagents could be used for the classification of 58 gammaA-myeloma proteins into two distinct antigenic types, respectively called subclasses He and Le. These differences were shown to be related to the heavy (alpha) polypeptide chains and independent of the integrity of interchain disulfide bridges. The gammaA-immunoglobulin from normal serum appears to consist, for the most part, of molecules with Le subclass specificity.     

Anti-idiotypic antibody vaccine for type B viral hepatitis in chimpanzees

Anti-idiotypic antibodies (anti-Id) that contain an internal image component that mimics the surface antigen of hepatitis B virus (HBsAg) were used to immunize chimpanzees. Four injections of the rabbit anti-Id preparation elicited an antibody response to HBsAg (anti-HBs). The antibody specificity appeared to be against the anti-Id, since the anti-Id immunogen was shown to bind the chimpanzee anti-HBs. Two chimpanzees immunized with the anti-Id, along with two control animals that were either untreated or received a nonimmune rabbit immunoglobulin G preparation, were challenged with infectious hepatitis B virus. Both control chimpanzees developed clinical and serological characteristics consistent with an active hepatitis B virus infection, whereas the two anti-Id treated chimpanzees were protected from infection. Since chimpanzees provide a relevant model of a human response to hepatitis B virus immunization and infection, these results indicate that anti-Id preparations such as that described here might be candidates for vaccines against human diseases.     

Alpha-chain disease: a new immunoglobulin abnormality

A new type of pathological immunoglobulin was found in the serum, urine, and saliva of a young Arab patient with abdominal lymphoma and diffuse lymphoplasmacytic infiltration of the small intestine. This protein is devoid of light chains and is closely related to the alpha polypeptide chains of the gamma(A1) (Le) subclass of immunoglobulin A. It is characterized by electrophoretic heterogeneity, tendency toward polymerization, and a high carbohydrate content. No intracellular synthesis of light chain was detected.